Conserved Protein Domain Family
C1_GMIP-like

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cd20816: C1_GMIP-like 
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family
The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Statistics
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PSSM-Id: 410366
Aligned: 46 rows
Threshold Bit Score: 66.8965
Created: 24-Oct-2019
Updated: 25-Oct-2021
Structure
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Aligned Rows:
 
Zn binding site
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:H C C C C H C CClick to see conserved feature residue pattern help
Evidence:
  • Comment:Two non-consecutive sets of zinc-binding residues form two separate metal-binding sites.
  • Comment:Based on the structure evidence that Rattus norvegicus ROCK2 binds two Zn2+ ions

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1           #            #  #          #  #    #  #       #    
Q92619        701 RTHRLRKLRT--PAKCRECNSYVYfQGAECEECCLACHKKCLETLAIqCGHKK 751  human
VDP05339      413 LSHRLQRTRA--PTKCCHCDSYTFfQTVQCTECGLAWHKACLGSVNFkCDSLR 463  Soboliphyme baturini
KHN81756      125 KSHRLQRIRQ--PTKCAHCEALSIlSTVQCAQCGMVWHKSCLARIAVfCGQSS 175  dog roundworm
VDD87846      371 GTHHFQKVRQ--PTRCVQCDAFSIfSTVQCTQCRLMWHKSCVPRISItCDQSM 421  human pinworm
PDM84927     1696 ASHSIQRTVQ--PGKCSHCDSISLlNSLQCSVCSLVWHKACFPQITVsCGHQT 1746 Pristionchus pacificus
CEF71204      569 KSHKLQRVRQ--PTKCSYCENISLlSTYQCTNCDTFYHKTCLSRLTAyCSEGR 619  Strongyloides ratti
XP_001748029  492 DMHAFVRLTI--PSKCKHCKRACYfNAFVCTKCHIACHRRCTEELEVrCNLAQ 542  Monosiga brevicollis MX1
XP_004989813  784 DMHSFARLNI--PSKCKCCKKACYfNSVVCSKCNLTCHKRCTEKLQApCPGSV 834  Salpingoeca rosetta
XP_009012426  428 NEHSFKALKI--PSKCRVCESYCCiTGLICTKCQICCHERCIYRLRFqCIGDG 478  Helobdella robusta
RWS25289       23 LTHTFTRIYSyvFERCRTCDAYIYlGGYKCEKCNLYSHSKCLKSVVIlCGQKP 75   Leptotrombidium deliense

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